Chlamydia trachomatis-derived deubiquitinating enzymes in mammalian cells during infection
about
The Genome of the Amoeba Symbiont "Candidatus Amoebophilus asiaticus" Reveals Common Mechanisms for Host Cell Interaction among Amoeba-Associated BacteriaRegulation and cellular roles of ubiquitin-specific deubiquitinating enzymesSubstrate specificity of the ubiquitin and Ubl proteasesSubverting Toll-Like Receptor Signaling by Bacterial PathogensConserved type III secretion system exerts important roles in Chlamydia trachomatisStructural analysis of Xanthomonas XopD provides insights into substrate specificity of ubiquitin-like protein proteasesCharacterization and structural studies of the Plasmodium falciparum ubiquitin and Nedd8 hydrolase UCHL3Identification by functional proteomics of a deubiquitinating/deNeddylating enzyme in Plasmodium falciparumDeubiquitinases: Novel Therapeutic Targets in Immune Surveillance?Characterisation of the Trichinella spiralis deubiquitinating enzyme, TsUCH37, an evolutionarily conserved proteasome interaction partnerDeubiquitinating enzymes as promising drug targets for infectious diseases.The chlamydial periplasmic stress response serine protease cHtrA is secreted into host cell cytosolMassive expansion of Ubiquitination-related gene families within the Chlamydiae.Antibiotic resistance in Chlamydiae.Corruption of innate immunity by bacterial proteases.Localization of Chlamydia trachomatis hypothetical protein CT311 in host cell cytoplasm.Ubiquitin-specific peptidase 5, a target molecule of vialinin A, is a key molecule of TNF-α production in RBL-2H3 cells.Identification of type III secretion substrates of Chlamydia trachomatis using Yersinia enterocolitica as a heterologous system.Chlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm.Chlamydia trachomatis secretion of hypothetical protein CT622 into host cell cytoplasm via a secretion pathway that can be inhibited by the type III secretion system inhibitor compound 1.Ubiquitin and ubiquitin-modified proteins activate the Pseudomonas aeruginosa T3SS cytotoxin, ExoU.Unity in variety--the pan-genome of the ChlamydiaeSseL, a Salmonella deubiquitinase required for macrophage killing and virulence.Chlamydia trachomatis In Vivo to In Vitro Transition Reveals Mechanisms of Phase Variation and Down-Regulation of Virulence FactorsElaD, a Deubiquitinating protease expressed by E. coliA functional ubiquitin-specific protease embedded in the large tegument protein (ORF64) of murine gammaherpesvirus 68 is active during the course of infectionDirectional evolution of Chlamydia trachomatis towards niche-specific adaptation.Transcription factor complex AP-1 mediates inflammation initiated by Chlamydia pneumoniae infection.Chlamydial intracellular survival strategies.Chlamydia cell biology and pathogenesisTrojan horse strategies used by pathogens to influence the small ubiquitin-like modifier (SUMO) system of host eukaryotic cellsImmune-mediated control of Chlamydia infection.Salmonella regulates polyubiquitination and surface expression of MHC class II antigens.Activity-based probes as a tool for functional proteomic analysis of proteases.New insights into Chlamydia intracellular survival mechanisms.New frontiers in type III secretion biology: the Chlamydia perspective.Chlamydia trachomatis-induced alterations in the host cell proteome are required for intracellular growth.Pathogenic Bacterial Proteins and their Anti-Inflammatory Effects in the Eukaryotic Host.Chlamydia trachomatis-containing vacuole serves as deubiquitination platform to stabilize Mcl-1 and to interfere with host defense.Bacterial proteases from the intracellular vacuole niche; protease conservation and adaptation for pathogenic advantage.
P2860
Q22065482-011C2787-056F-41FE-835C-068A3D59B6FFQ24645701-3150B85B-7341-4C0F-9859-8169B1343048Q26751372-D8A63AC3-BC13-402B-86D7-3BB78C581C90Q26773133-6AEEC938-D3B7-4268-A8CC-2070915ECEB0Q26998512-6502358F-121B-4948-8FF0-7A00E2A1D9EDQ27643481-0CE3BB3A-27CE-4AB4-BBCA-A1E004E69314Q27658820-3FD60C19-CC41-4B7C-B06E-EB033B1142CDQ27972596-68C2D945-5A3D-4A3D-B3A0-4FE149EE4979Q28069021-FEDC0006-8C8F-4D92-B5C7-D8664D08EF43Q28477341-2AC73888-33FC-47BD-B694-9CC38EA0ADDCQ33836097-2AEA405D-BE10-47AD-8F46-0EE1279B2AEBQ33884136-A2CB8CCC-3B26-40F6-A61C-60FD606FDD9CQ34402710-B7FEBD3F-A8F4-4719-BAE8-508004D232ABQ34784830-FFFB12A4-D7F2-4440-B086-54EB6845130FQ35003110-8E53C8FF-069A-4633-8B4F-82069885E303Q35061773-EDA94885-4255-42CD-BF9A-C52F73BE896CQ35069450-86285F9A-FE24-44F3-80DD-6940C60158FFQ35095777-EA4AA023-2BD8-4328-BBAF-94950BDBC88CQ35096129-4B5091B9-2C1A-41D9-9D68-9D9143E83CFBQ35114743-3A6D7B76-E02F-4FA7-B165-6EA30357F894Q35613242-1DF1167B-F8A1-4FE0-82AB-AE92D8E80B3FQ35639106-3427A265-3575-4400-AE9E-4FBBBB6E8F59Q35645616-4C155480-371D-4323-A4A6-3579A674DCDFQ35710313-A681FA95-944B-4DFA-906E-9AD7C9E78714Q35741864-53C40DB1-11D3-4F68-83DA-B1359395A5F5Q36099153-BDE3AADB-94BA-41F1-ACA8-99F636CE8D3DQ36363498-33CDEC92-EA52-487E-994C-A1B5218B643CQ36673413-72E245B6-8E29-42FF-9204-C9D722F253ACQ36786613-0A4B3944-95BB-4ABC-A13D-45A33CE202E3Q36950792-01A3B088-3843-4287-B227-94B1A864211BQ36966125-9A986933-60B8-4F41-B268-FB071F81838BQ36990773-2F2DA6C0-7940-4FC4-B4E2-F5E4F6627BB6Q37291725-40D9A0CE-4116-4F6A-957B-DCFC0D9B9872Q37304140-0B8D4D25-6ACD-4D91-A5E7-8B3BE1F5E810Q37453342-871D9219-119F-40C8-B9E8-2938E72D3236Q37548120-C7F8C038-7A03-491B-ACAB-010C0035F75FQ37598672-7C00FA8D-AB3A-4999-A935-45329391114FQ37678929-58629C50-97D4-4D27-8E05-253F774DC924Q37725770-B60E482C-4799-4D82-B9B0-B2CD3681A78CQ37733692-81A8FB17-3838-4135-B48E-1B6B56959880
P2860
Chlamydia trachomatis-derived deubiquitinating enzymes in mammalian cells during infection
description
2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2006
@ast
im Juli 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2006/07/01)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/07/01)
@nl
наукова стаття, опублікована в липні 2006
@uk
مقالة علمية (نشرت في يوليو 2006)
@ar
name
Chlamydia trachomatis-derived ...... mmalian cells during infection
@ast
Chlamydia trachomatis-derived ...... mmalian cells during infection
@en
Chlamydia trachomatis-derived ...... mmalian cells during infection
@nl
type
label
Chlamydia trachomatis-derived ...... mmalian cells during infection
@ast
Chlamydia trachomatis-derived ...... mmalian cells during infection
@en
Chlamydia trachomatis-derived ...... mmalian cells during infection
@nl
prefLabel
Chlamydia trachomatis-derived ...... mmalian cells during infection
@ast
Chlamydia trachomatis-derived ...... mmalian cells during infection
@en
Chlamydia trachomatis-derived ...... mmalian cells during infection
@nl
P2093
P2860
P3181
P1476
Chlamydia trachomatis-derived ...... mmalian cells during infection
@en
P2093
Andre Catic
Eric Spooner
Hidde L. Ploegh
Michael N. Starnbach
Shahram Misaghi
Zarine R. Balsara
P2860
P304
P3181
P356
10.1111/J.1365-2958.2006.05199.X
P407
P577
2006-07-01T00:00:00Z